FORMAZIONE
2007: Laurea in Chimica e Tecnologie Farmaceutiche, Università di Padova. Relatore di tesi Prof. Stefano Moro
2011: Dottorato di ricerca in Biochimica e Biotechnologie (ind. Biotechnologie), Università di Padova. Supervisore Prof. Stefano Mammi

POSIZIONE ATTUALE
Professore Asoociato (SSD CHIM/08)

ESPERIENZE LAVORATIVE
-2007: Borsista, Dipartimento di Scienze Farmaceutiche, Università di Padova. Supervisori: Prof. Stefano Moro and Dr Alessandro Padova (SienaBiotech).
-2010: Visiting PhD, Sanford|Burnham Medical Research Institute, La Jolla, CA, USA. Supervisore: Prof. Maurizio Pellecchia
-2011-2013: Assegnista di ricerca, Dipartimento di Scienze Chimiche, Università di Padova. Supervisore: Prof. Massimo Bellanda
-2014-2016: Assegnista di ricerca Senior, Dipartimento di Scienze del Farmaco, Università di Padova. Supervisore: Prof. Stefano Moro
-2017-2020: Ricercatore RTD-A (SSD CHIM/08)
-2020-2023: Ricercatore RTD-B (SSD CHIM/08)


RESPONSABILITA' FINANZIAMENTI
-2018-2020: STARS Grants call 2017, Università di Padova.
Project Title:"A novel strategy to speed up fragment-based drug discovery combining Supervised Molecular Dynamics with NMR data."
-2017-2019: PRID-J, Dipartimento di Scienze del Farmaco. Università di Padova.
Project Title: “Design of novel BCL-2 family inhibitors by using fragment-based drug discovery by NMR approach”
-2014: Grant by BIONMR (FP7) (BIO-NMR-00247). Project Title: ”Structure determination of the TxrCP4 from Echinococcusgranulosus.”
-2013-2015: Grant "Progetto Giovani Studiosi 2013", Università di Padova.

ATTIVITA' DIDATTICA
AA 2016/17-oggi: ANALISI DEI FARMACI I (M-Z)

10 pubblicazioni piu' recenti:
1. Sturlese M, Manta B, Bertarello A, Bonilla M, Lelli M, Zambelli B, Grunberg K, Mammi S, Comini MA, Bellanda M (2018) The lineage-specific, intrinsically disordered N-terminal extension of monothiol glutaredoxin 1 from trypanosomes contains a regulatory region. Sci Rep; 8: 13716.

2. Farina B, Sturlese M, Mascanzoni F, Caporale A, Monti A, Di Sorbo G, Fattorusso R, Ruvo M, Doti N (2018) Binding mode of AIF(370-394) peptide to CypA: insights from NMR, label-free and molecular docking studies. Biochem J; 475: 2377–2393.

3. Cuzzolin A, Deganutti G, Salmaso V, Sturlese M, Moro S (2018) AquaMMapS: An Alternative Tool to Monitor the Role of Water Molecules During Protein-Ligand Association. ChemMedChem; 13: 522–531.

4. Bortolozzi R, Mattiuzzo E, Dal Pra M, Sturlese M, Moro S, Hamel E, Carta D, Viola G, Ferlin MG (2018) Targeting tubulin polymerization by novel 7-aryl-pyrroloquinolinones: Synthesis, biological activity and SARs. Eur J Med Chem; 143: 244–258.

5. Salmaso V, Sturlese M, Cuzzolin A, Moro S (2018) Combining self- and cross-docking as benchmark tools: the performance of DockBench in the D3R Grand Challenge 2. J Comput Aided Mol Des; 32: 251–264.

6. Sabbadin D, Salmaso V, Sturlese M, Moro S (2018) Supervised molecular dynamics (sumd) approaches in drug design. Methods Mol Biol. 2018; 1824 287-298

7. Squarcialupi L, Betti M, Catarzi D, Varano F, Falsini M, Ravani A, Pasquini S, Vincenzi F, Salmaso V, Sturlese M, Varani K, Moro S, Colotta V (2017) The role of 5-arylalkylamino- and 5-piperazino- moieties on the 7-aminopyrazolo[4,3-d]pyrimidine core in affecting adenosine A1 and A2A receptor affinity and selectivity profiles. J Enzyme Inhib Med Chem; 32: 248–263.

8. Malvacio I, Cuzzolin A, Sturlese M, Vera DMA, Moyano EL, Moro S (2017) Synthesis and preliminary structure-activity relationship study of 2-aryl-2H-pyrazolo[4,3-c]quinolin-3-ones as potential checkpoint kinase 1 (Chk1) inhibitors. J Enzyme Inhib Med Chem; 33: 171–183.

9. Manta B, Bonilla M, Fiestas L, Sturlese M, Salinas G, Bellanda M, Comini MA (2017) Polyamine-Based Thiols in Trypanosomatids: Evolution, Protein Structural Adaptations, and Biological Functions. Antioxid Redox Signal; doi:10.1089/ars.2017.7133.

10. Bertini S, Ghilardi E, Asso V, Minutolo F, Rapposelli S, Digiacomo M, Saccomanni G, Salmaso V, Sturlese M, Moro S, Macchia M, Manera C (2017) Sulfonamido-derivatives of unsubstituted carbazoles as BACE1 inhibitors. Bioorg Med Chem Lett; 27: 4812–4816.

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BRIEF DESCRIPTION:
The scientific interests of Dr Sturlese are in the field of the recognition between small molecules and peptides with proteins, with the goal to investigate the molecular basis of the interaction processes to rationally design specific products and drugs.
He has also solved several proteins and peptides structures utilizing nuclear magnetic resonance (NMR) spectroscopy applying the most modern techniques (3D experiments, Sparse Sampling, and Fast Multidimensional NMR) to the conformational study of proteins. In particular, he has focused his attention on the use of NMR in Drug Discovery (e.g. Fragment-Based Drug Discovery, Protein-Ligand complex elucidation, binding affinity estimation) with a particular attention to cancer research.
Dr Sturlese is also involved in the development of new computational strategy to interpret and maximize the information obtained by NMR experiments. Examples of this hybrid approach are: (i) steer molecular docking by Ligand-based or Protein-based NMR signals; (ii) coupling Molecular Dynamics Simulations with chemical shit data.
Part of the scientific activity of Dr Sturlese is devoted to the production of recombinant proteins (Isotope-labeling, residue-specific-labelling, reverse-specific-labelling).

TECHNICAL EXPERTISE:
-Protein-NMR: Drug discovery by NMR, Multidimensional (1D,2D,3D) and hetero-nuclear spectra acquisition, processing and analysis. Peptide and Protein NMR Assignment (homonuclear and heteronuclear assignment), Peptide and Protein NMR structure determination.
-Molecular Biology: Protein production using E.Coli expression host, Isotope-labeling (15N, 13C), residue-specific-labeling, reverse-specific-labeling. Phage Display.
-Molecular Modeling: Structure-based and ligand-based drug design, molecular docking and virtual screening, Molecular Dynamics, Quantum Mechanical Calculation, and Programming.

-Fragment-based Drug Discovery tramite NMR in ambito oncologico.
-Caratterizzazione delle modalità di interazione Proteina-Ligando e Peptide-Proteina tramite NMR e metodi computazionali.
-Espressione e Purificazione di Proteine ricombinanti per screening di frammenti.